Article abstract
Nature Immunology 8, 975 - 983 (2007)
Published online: 12 August 2007 | doi:10.1038/ni1502
Structural evidence for a germline-encoded T cell receptor–major histocompatibility complex interaction 'codon'
Dan Feng1, Christopher J Bond1, Lauren K Ely1, Jennifer Maynard1,2 & K Christopher Garcia1
Abstract
All complexes of T cell receptors (TCRs) bound to peptide–major histocompatibility complex (pMHC) molecules assume a stereotyped binding 'polarity', despite wide variations in TCR-pMHC docking angles. However, existing TCR-pMHC crystal structures have failed to show broadly conserved pairwise interaction motifs. Here we determined the crystal structures of two TCRs encoded by the variable 
-chain 8.2 (V
8.2), each bound to the MHC class II molecule I-Au, and did energetic mapping of V
and V contacts with I-Au. Together with two previously solved structures of V8.2-containing TCR-MHC complexes, we found four TCR–I-A complexes with structurally superimposable interactions between the V loops and the I-A 
-helix. This examination of a narrow 'slice' of the TCR-MHC repertoire demonstrates what is probably one of many germline-derived TCR-MHC interaction 'codons'.
- Howard Hughes Medical Institute, Department of Molecular & Cellular Physiology, Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, USA.
- Present address: Department of Chemical Engineering, University of Texas at Austin, Austin, Texas 78712, USA.
Correspondence to: K Christopher Garcia1 e-mail: kcgarcia@stanford.edu
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